Copper in PDB 5z62: Structure of Human Cytochrome C Oxidase
Enzymatic activity of Structure of Human Cytochrome C Oxidase
All present enzymatic activity of Structure of Human Cytochrome C Oxidase:
1.9.3.1;
Other elements in 5z62:
The structure of Structure of Human Cytochrome C Oxidase also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Structure of Human Cytochrome C Oxidase
(pdb code 5z62). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the
Structure of Human Cytochrome C Oxidase, PDB code: 5z62:
Jump to Copper binding site number:
1;
2;
3;
Copper binding site 1 out
of 3 in 5z62
Go back to
Copper Binding Sites List in 5z62
Copper binding site 1 out
of 3 in the Structure of Human Cytochrome C Oxidase
 Mono view
 Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Structure of Human Cytochrome C Oxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu601
b:65.3
occ:1.00
|
ND1
|
A:HIS240
|
2.1
|
62.3
|
1.0
|
NE2
|
A:HIS291
|
2.1
|
58.3
|
1.0
|
NE2
|
A:HIS290
|
2.1
|
62.2
|
1.0
|
CE1
|
A:HIS240
|
2.8
|
62.3
|
1.0
|
CE1
|
A:HIS291
|
3.0
|
58.3
|
1.0
|
CE1
|
A:HIS290
|
3.0
|
62.2
|
1.0
|
CG
|
A:HIS240
|
3.1
|
62.3
|
1.0
|
CD2
|
A:HIS291
|
3.1
|
58.3
|
1.0
|
CD2
|
A:HIS290
|
3.1
|
62.2
|
1.0
|
CB
|
A:HIS240
|
3.6
|
62.3
|
1.0
|
NE2
|
A:HIS240
|
3.8
|
62.3
|
1.0
|
CD2
|
A:HIS240
|
4.0
|
62.3
|
1.0
|
ND1
|
A:HIS291
|
4.1
|
58.3
|
1.0
|
ND1
|
A:HIS290
|
4.1
|
62.2
|
1.0
|
CG
|
A:HIS291
|
4.2
|
58.3
|
1.0
|
CA
|
A:HIS240
|
4.2
|
62.3
|
1.0
|
CG
|
A:HIS290
|
4.2
|
62.2
|
1.0
|
FE
|
A:HEA604
|
4.5
|
58.4
|
1.0
|
C1A
|
A:HEA604
|
4.6
|
58.4
|
1.0
|
ND
|
A:HEA604
|
4.7
|
58.4
|
1.0
|
NA
|
A:HEA604
|
4.8
|
58.4
|
1.0
|
C2A
|
A:HEA604
|
4.8
|
58.4
|
1.0
|
C4A
|
A:HEA604
|
4.9
|
58.4
|
1.0
|
C4D
|
A:HEA604
|
4.9
|
58.4
|
1.0
|
CG2
|
A:VAL243
|
5.0
|
57.0
|
1.0
|
CHA
|
A:HEA604
|
5.0
|
58.4
|
1.0
|
C3A
|
A:HEA604
|
5.0
|
58.4
|
1.0
|
N
|
A:HIS240
|
5.0
|
62.3
|
1.0
|
|
Copper binding site 2 out
of 3 in 5z62
Go back to
Copper Binding Sites List in 5z62
Copper binding site 2 out
of 3 in the Structure of Human Cytochrome C Oxidase
 Mono view
 Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Structure of Human Cytochrome C Oxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu301
b:0.0
occ:1.00
|
CU
|
B:CU302
|
1.2
|
0.2
|
1.0
|
ND1
|
B:HIS161
|
2.2
|
70.6
|
1.0
|
SG
|
B:CYS200
|
2.4
|
71.6
|
1.0
|
SG
|
B:CYS196
|
2.4
|
74.2
|
1.0
|
CE1
|
B:HIS161
|
2.9
|
70.6
|
1.0
|
SD
|
B:MET207
|
2.9
|
72.4
|
1.0
|
CB
|
B:CYS200
|
3.2
|
71.6
|
1.0
|
CG
|
B:HIS161
|
3.3
|
70.6
|
1.0
|
O
|
B:GLU198
|
3.5
|
71.1
|
1.0
|
CE
|
B:MET207
|
3.5
|
72.4
|
1.0
|
CB
|
B:CYS196
|
3.6
|
74.2
|
1.0
|
ND1
|
B:HIS204
|
3.7
|
67.5
|
1.0
|
CB
|
B:HIS161
|
3.9
|
70.6
|
1.0
|
CA
|
B:HIS161
|
4.1
|
70.6
|
1.0
|
NE2
|
B:HIS161
|
4.1
|
70.6
|
1.0
|
CG
|
B:MET207
|
4.1
|
72.4
|
1.0
|
CE1
|
B:HIS204
|
4.3
|
67.5
|
1.0
|
CD2
|
B:HIS161
|
4.3
|
70.6
|
1.0
|
O
|
B:LEU160
|
4.5
|
70.5
|
1.0
|
CA
|
B:CYS200
|
4.5
|
71.6
|
1.0
|
N
|
B:CYS200
|
4.6
|
71.6
|
1.0
|
C
|
B:GLU198
|
4.7
|
71.1
|
1.0
|
CG
|
B:HIS204
|
4.9
|
67.5
|
1.0
|
CA
|
B:HIS204
|
5.0
|
67.5
|
1.0
|
|
Copper binding site 3 out
of 3 in 5z62
Go back to
Copper Binding Sites List in 5z62
Copper binding site 3 out
of 3 in the Structure of Human Cytochrome C Oxidase
 Mono view
 Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Structure of Human Cytochrome C Oxidase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu302
b:0.2
occ:1.00
|
CU
|
B:CU301
|
1.2
|
0.0
|
1.0
|
SG
|
B:CYS200
|
2.4
|
71.6
|
1.0
|
SG
|
B:CYS196
|
2.4
|
74.2
|
1.0
|
SD
|
B:MET207
|
2.5
|
72.4
|
1.0
|
ND1
|
B:HIS204
|
3.0
|
67.5
|
1.0
|
CB
|
B:CYS196
|
3.0
|
74.2
|
1.0
|
CG
|
B:MET207
|
3.3
|
72.4
|
1.0
|
ND1
|
B:HIS161
|
3.3
|
70.6
|
1.0
|
CE
|
B:MET207
|
3.5
|
72.4
|
1.0
|
CB
|
B:CYS200
|
3.7
|
71.6
|
1.0
|
CE1
|
B:HIS204
|
3.7
|
67.5
|
1.0
|
CE1
|
B:HIS161
|
3.8
|
70.6
|
1.0
|
O
|
B:HIS204
|
3.8
|
67.5
|
1.0
|
O
|
B:GLU198
|
3.9
|
71.1
|
1.0
|
CA
|
B:HIS204
|
4.0
|
67.5
|
1.0
|
CG
|
B:HIS204
|
4.1
|
67.5
|
1.0
|
CB
|
B:HIS204
|
4.4
|
67.5
|
1.0
|
C
|
B:HIS204
|
4.4
|
67.5
|
1.0
|
CG
|
B:HIS161
|
4.5
|
70.6
|
1.0
|
CA
|
B:CYS196
|
4.5
|
74.2
|
1.0
|
N
|
B:CYS200
|
4.7
|
71.6
|
1.0
|
CB
|
B:MET207
|
4.7
|
72.4
|
1.0
|
CA
|
B:CYS200
|
4.8
|
71.6
|
1.0
|
O
|
B:ASN203
|
4.9
|
70.3
|
1.0
|
NE2
|
B:HIS204
|
5.0
|
67.5
|
1.0
|
CB
|
B:HIS161
|
5.0
|
70.6
|
1.0
|
|
Reference:
S.Zong,
M.Wu,
J.Gu,
T.Liu,
R.Guo,
M.Yang.
Structure of the Intact 14-Subunit Human Cytochrome C Oxidase. Cell Res. V. 28 1026 2018.
ISSN: ISSN 1748-7838
PubMed: 30030519
DOI: 10.1038/S41422-018-0071-1
Page generated: Wed Jul 31 05:33:59 2024
|